NorthShore University HealthSystem Research Institute is seeking a company to license and/or co-develop a promising therapeutic target for tumor growth and metastasis, wound healing, and other pathological conditions. Research Institute researchers have identified that h2-caponin is a crucial cytoskeleton protein in modulating the processes of cell proliferation and migration.
H2-calponin is a novel target for developing new treatments for cancer, atherosclerosis, automimmune diseases, improving wound healing, improving lung protection, promoting bone formation, and promoting myogenesis and tissue repair. Although widely expressed, coupled with the appropriate organ-specific carriers, H2-Calponin provides numerous promising pathways for development.
- A novel approach to inhibit cell proliferation as therapeutic treatment for cancer growth and metastasis, myeloid leukemia, atherosclerosis and other diseases.
- Highly specific target that will not interfere with all cellular function.
Calponin is an actin filament associated regulatory protein. H2-calponin is a member of the calponin family. H2-calponin is found in smooth muscle and a number of non-muscle cells such as epidermal karetinocytes, lung alveolar cells, cornea epithelial cells, vascular endothelial cells, kidney podocytes, osteoblasts, fibroblasts, monocytes/macrophages, neutrophils, myoblasts, embryonic stem cells, and a number of cancer cells including breast cancer, prostate cancer and colon cancer cells. We previously showed that transfective (unregulated) over-expression of h2-calponin inhibited cell proliferation (Hossain et al., 2003). Unregulated over-expression also inhibits cell migration. In our newly developed h2-calponin gene knock out/knock down mice, we recently found that the diminished expression and function of h2-calponin also alters cell migration and proliferation (Hossain et al., 2007 Meeting abstract). Therefore, targeting h2-calponin expression level (e.g., by transfective over-expression or RNAi inhibition) and function (e.g., PKC phosphorylation) may be able to control the proliferation and migration of the above cell types for treatment purposes. One of our novel findings is that H2-calponin is regulated by mechanical tension at the level of gene expression as well as proteolytic degradation (Hossain et al., 2005; 2006). Therefore, by controlling h2-calponin level and function, we may be able to alter mechanical tension related processes, such as skin wound healing and lung preservation during prolonged deflation , as well as prevent metastasis in cancer cells.
Patent Status: Patent Pending
About The Inventor
Jian-Ping Jin, PhD, is the former Section Chief of Molecular Cardiology for NorthShore Research Institute (currently Chairman of the Department of Physiology of Wayne State University). His research is focused on the gene regulation and structure-function relationships of muscle proteins. He has been published more than eighty times in various peer reviewed journals and press. Dr. Jin is currently a Standing Member of a grant review panel at National Institutes of Health. He is a Member of the Editorial Board of Archives of Biochemistry and Biophysics and the Guest Editor of the 2006 Highlight Issue in Contractile Proteins.
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